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Yorodumi- PDB-4ctm: Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Rin... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4ctm | ||||||
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Title | Glucopyranosylidene-spiro-iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation as Glycogen Phosphorylase Inhibitors by Enzyme Kinetic and Crystallographic Methods | ||||||
Components | GLYCOGEN PHOSPHORYLASE, MUSCLE FORM | ||||||
Keywords | TRANSFERASE / TYPE 2 DIABETES / INHIBITOR / STRUCTURE-BASED DRUG DESIGN | ||||||
Function / homology | Function and homology information glycogen phosphorylase / glycogen phosphorylase activity / linear malto-oligosaccharide phosphorylase activity / SHG alpha-glucan phosphorylase activity / glycogen catabolic process / skeletal muscle myofibril / pyridoxal phosphate binding / nucleotide binding Similarity search - Function | ||||||
Biological species | ORYCTOLAGUS CUNICULUS (rabbit) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å | ||||||
Authors | Alexacou, K.M. / Papakonstantinou, M. / Leonidas, D.D. / Zographos, S.E. / Chrysina, E.D. | ||||||
Citation | Journal: Bioorg.Med.Chem. / Year: 2014 Title: Glucopyranosylidene-Spiro-Iminothiazolidinone, a New Bicyclic Ring System: Synthesis, Derivatization, and Evaluation for Inhibition of Glycogen Phosphorylase by Enzyme Kinetic and Crystallographic Methods. Authors: Czifrak, K. / Deak, S. / Pahi, A. / Kover, K.E. / Docsa, T. / Gergely, P. / Alexacou, K.M. / Papakonstantinou, M. / Leonidas, D.D. / Zographos, S.E. / Chrysina, E.D. / Somsak, L. #1: Journal: Protein Sci. / Year: 1998 Title: The Structure of a Glycogen Phosphorylase Glucopyranose Spirohydantoin Complex at 1.8 A Resolution and 100 K: The Role of the Water Structure and its Contribution to Binding. Authors: Gregoriou, M. / Noble, M.E. / Watson, K.A. / Garman, E.F. / Krulle, T.M. / De La Fuente, C. / Fleet, G.W. / Oikonomakos, N.G. / Johnson, L.N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ctm.cif.gz | 180.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ctm.ent.gz | 141.2 KB | Display | PDB format |
PDBx/mmJSON format | 4ctm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ct/4ctm ftp://data.pdbj.org/pub/pdb/validation_reports/ct/4ctm | HTTPS FTP |
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-Related structure data
Related structure data | 4ctnC 4ctoC 2pydS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 97422.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ORYCTOLAGUS CUNICULUS (rabbit) / Organ: MUSCLESkeletal muscle / Tissue: MUSCLESkeletal muscle / References: UniProt: P00489, glycogen phosphorylase |
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#2: Chemical | ChemComp-MIF / ( |
#3: Chemical | ChemComp-PLP / |
#4: Chemical | ChemComp-PO4 / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.95 % / Description: NONE |
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Crystal grow | pH: 6.8 Details: 25MG/ML ENZYME, 1MM SPERMINE, 10MM BES, 3MM DTT, 0.1MM EDTA, 0.02% SODIUM AZIDE, PH 6.7 |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: SYNCHROTRON / Site: SRS / Beamline: PX10.1 / Wavelength: 0.97976 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Nov 16, 2007 / Details: MIRRORS |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97976 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→35.7 Å / Num. obs: 69137 / % possible obs: 98 % / Observed criterion σ(I): 0 / Redundancy: 5.3 % / Biso Wilson estimate: 25.4 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 20.4 |
Reflection shell | Resolution: 1.95→2.06 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.38 / Mean I/σ(I) obs: 5.1 / % possible all: 96.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2PYD Resolution: 1.95→35.71 Å / Cor.coef. Fo:Fc: 0.967 / Cor.coef. Fo:Fc free: 0.958 / SU B: 2.873 / SU ML: 0.083 / Cross valid method: THROUGHOUT / ESU R: 0.147 / ESU R Free: 0.127 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.349 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→35.71 Å
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